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ATG12–ATG5-TECPR1: an alternative E3-like complex utilized during the cellular response to lysosomal membrane damage
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).ORCID iD: 0000-0001-7930-0134
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).ORCID iD: 0000-0002-2573-8736
2024 (English)In: Autophagy, ISSN 1554-8627, E-ISSN 1554-8635, Vol. 20, no 2, p. 443-444Article in journal (Refereed) Published
Abstract [en]

ATG16L1 is an essential component of the Atg8-family protein conjugation machinery, providing membrane targeting for the ATG12–ATG5 conjugate. Recently, we identified an alternative E3-like complex that functions independently of ATG16L1. This complex utilizes the autophagosome-lysosome tethering factor TECPR1 for membrane targeting. TECPR1 is recruited to damaged lysosomal membranes via a direct interaction with sphingomyelin. At the damaged membrane, TECPR1 assembles into an E3-like complex with ATG12–ATG5 to regulate unconventional LC3 lipidation and promote efficient lysosomal repair.

Place, publisher, year, edition, pages
Taylor & Francis, 2024. Vol. 20, no 2, p. 443-444
Keywords [en]
ESCRT, lysophagy, lysosome, membrane repair, TECPR1
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-215934DOI: 10.1080/15548627.2023.2267414ISI: 001095815100001PubMedID: 37872727Scopus ID: 2-s2.0-85174580555OAI: oai:DiVA.org:umu-215934DiVA, id: diva2:1809175
Funder
EU, European Research CouncilGöran Gustafsson Foundation for Research in Natural Sciences and MedicineKnut and Alice Wallenberg FoundationSwedish Research Council, 2018-04585Swedish Research Council, 2022-02932Available from: 2023-11-02 Created: 2023-11-02 Last updated: 2024-04-26Bibliographically approved

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Corkery, Dale P.Wu, Yao-Wen

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